A pathway for the interconversion of hexose and pentose in the parasitic amoeba Entamoeba histolytica
- 15 April 1982
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 204 (1), 191-199
- https://doi.org/10.1042/bj2040191
Abstract
Isotope studies indicate that hexose-to-pentose interconversion by axenic Entamoeba histolytica conserves the C-1 and C-6 hexose carbon atoms. Transketolase was readily identified in amoebal extracts, and transaldolase could not be demonstrated. However, sedoheptulose 7-phosphate is a substrate for the PPi-dependent amoebal phosphofructokinase, and sedoheptulose 1,7-bisphosphate is cleaved by amoebal aldolase to dihydroxyacetone phosphate and erythrose phosphate. Since these three enzymes catalyse physiologically reversible reactions, a non-oxidative pathway for hexose-pentose interconversion exists in amoebae in the absence of transaldolase. By using known amoebal enzyme, the conversion of ribose into fructose was confirmed in vitro. Some kinetic parameters of amoebal phosphofructokinase, transketolase and aldolase were determined.This publication has 20 references indexed in Scilit:
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